During the process of protein translocation, the asparagine residues in Asn-x-Ser/Thr motifs on the nascent polypeptide chain are glycosylated in the lumen of the ER by a multisubunit membrane protein complex called oligosaccharyltransferase (OST).
Oligosaccharides are cleaved into monosaccharides by enzyme complexes called alpha-glucosidases, which are present in the brush border membrane of the small intestine.
Cell-to-cell adhesion complexes called adherens junctions contain proteins such as catenins, which are bound to membrane cadherins and intracellular actin.
The fusion of these vesicles is mediated by protein complexes called SNAREs (El Kasmi et al., 2013), whilst clathrin-coated vesicles mediate the endocytosis of excess membrane material away from the cell plate (Jürgens, 2005).
In the vicinity of the plasma membrane, the octameric complex called exocyst will serve as a tether to keep the vesicle in close relationship with the plasma membrane and facilitating the membrane fusion by the formation of the SNARE complex prior to the release of the vesicle cargo.
Some proteins have to be inserted into the membranes of cells and these proteins are directed, as they are being built, to the membrane by another molecular complex called the signal recognition particle (or SRP for short).
Because in schizonts and gametocytes before activation the PfGAP50 is part of the actin-myosin motor complex driven invasion machinery (glideosome) associated to the multi-protein complex called inner membrane complex (IMC), the cell membranes were permeabilized by saponin washing upon preparation of these samples.
Bacteroides thetaiotaomicron, found in the distal intestine (colon) of the GI-tract, has an outer-membrane-associated multi-protein complex called the starch-utilization system (Sus), consisting of different starch-binding proteins and sugar degradation enzymes encoded in gene clusters [ 54- 57].
PfGAP50, a 44.6 kDa transmembrane protein, forms an essential part of the actin-myosin motor complex driven invasion machinery (glideosome) associated to the multi-protein complex called inner membrane complex (IMC) [ 20– 23].
